MED28_ARATH
ID MED28_ARATH Reviewed; 156 AA.
AC Q9LFA5;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 28 {ECO:0000303|PubMed:17560376};
GN Name=MED28 {ECO:0000303|PubMed:17560376};
GN Synonyms=MED28_1 {ECO:0000303|PubMed:22021418};
GN OrderedLocusNames=At3g52860 {ECO:0000312|Araport:AT3G52860};
GN ORFNames=F8J2.30 {ECO:0000312|EMBL:CAB86890.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND NOMENCLATURE.
RX PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT as the Med25 subunit.";
RL Mol. Cell 26:717-729(2007).
RN [6]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=22021418; DOI=10.1104/pp.111.188300;
RA Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
RT "The Mediator complex in plants: structure, phylogeny, and expression
RT profiling of representative genes in a dicot (Arabidopsis) and a monocot
RT (rice) during reproduction and abiotic stress.";
RL Plant Physiol. 157:1609-1627(2011).
RN [7]
RP SUBUNIT, MUTAGENESIS OF CYS-44 AND CYS-55, AND INTERACTION WITH GEBPL.
RX PubMed=25877331; DOI=10.1042/bj20150132;
RA Shaikhali J., Davoine C., Braennstroem K., Rouhier N., Bygdell J.,
RA Bjoerklund S., Wingsle G.;
RT "Biochemical and redox characterization of the mediator complex and its
RT associated transcription factor GeBPL, a GLABROUS1 enhancer binding
RT protein.";
RL Biochem. J. 468:385-400(2015).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. The Mediator complex, having a compact
CC conformation in its free form, is recruited to promoters by direct
CC interactions with regulatory proteins and serves for the assembly of a
CC functional pre-initiation complex with RNA polymerase II and the
CC general transcription factors.
CC -!- SUBUNIT: Dimers (PubMed:25877331). Component of the Mediator complex
CC (PubMed:17560376). Interacts with GEBPL (PubMed:25877331).
CC {ECO:0000269|PubMed:17560376, ECO:0000269|PubMed:25877331}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 28 family.
CC {ECO:0000305}.
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DR EMBL; AL132969; CAB86890.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79001.1; -; Genomic_DNA.
DR EMBL; BT005037; AAO50570.1; -; mRNA.
DR EMBL; AK117706; BAC42357.1; -; mRNA.
DR PIR; T47543; T47543.
DR RefSeq; NP_190854.1; NM_115146.6.
DR AlphaFoldDB; Q9LFA5; -.
DR SMR; Q9LFA5; -.
DR IntAct; Q9LFA5; 1.
DR STRING; 3702.AT3G52860.1; -.
DR PaxDb; Q9LFA5; -.
DR PRIDE; Q9LFA5; -.
DR ProteomicsDB; 238254; -.
DR EnsemblPlants; AT3G52860.1; AT3G52860.1; AT3G52860.
DR GeneID; 824452; -.
DR Gramene; AT3G52860.1; AT3G52860.1; AT3G52860.
DR KEGG; ath:AT3G52860; -.
DR Araport; AT3G52860; -.
DR TAIR; locus:2085156; AT3G52860.
DR eggNOG; ENOG502RZ9Y; Eukaryota.
DR HOGENOM; CLU_1789747_0_0_1; -.
DR InParanoid; Q9LFA5; -.
DR OMA; EDMISWV; -.
DR OrthoDB; 1557970at2759; -.
DR PhylomeDB; Q9LFA5; -.
DR PRO; PR:Q9LFA5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LFA5; baseline and differential.
DR Genevisible; Q9LFA5; AT.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:1900055; P:regulation of leaf senescence; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR034456; MED28.
DR PANTHER; PTHR39117; PTHR39117; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..156
FT /note="Mediator of RNA polymerase II transcription subunit
FT 28"
FT /id="PRO_0000418356"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..156
FT /evidence="ECO:0000255"
FT COMPBIAS 10..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 44
FT /note="C->S: Loss of oligomerization. Loss of
FT oligomerization and dimerization; when associated with S-
FT 55."
FT /evidence="ECO:0000269|PubMed:25877331"
FT MUTAGEN 55
FT /note="C->S: Loss of oligomerization. Loss of
FT oligomerization and dimerization; when associated with S-
FT 44."
FT /evidence="ECO:0000269|PubMed:25877331"
SQ SEQUENCE 156 AA; 17961 MW; 43C35226F4041346 CRC64;
MDYQQKPPQS SDPSPSPPDR PPGIRSPETP SNNQNNDIED IMACVTALEA ALLPCLPARE
LQAIDRSPHP SHQIDVERHA RDFMEAAKKL QLYFMGLKRE DRAPSRAESL KKDIAVMEEE
LKTKDELIKK HMRLFQESQK LVKEQIEKHR DELEKV
